Aspartate protease

Aspartate (or Carboxylproteasen ) are enzymes capable of cleaving peptide bonds of a protein (protein ) ( proteolysis ), wherein one molecule of water is consumed (hydrolysis ), and the water molecule from the amino acid aspartic acid is retained in position, is part of the protease and at the same time constitutes the catalytic site. It is in aspartic proteases consistently to endopeptidases.

Classification according to UniProt / MEROPS

The UniProt Consortium regularly publishes a list of peptidases which categorizes these enzymes according to their evolutionary descent. The data in the list are provided with quality information, in the MEROPS database available. Closely related molecules are grouped into families whose identifiers consist of a letter ('A' for aspartate ) and a number. Families in turn belong to clans whose families are related. Clan identifiers instead of numbers have a letter.

There are 15 aspartic protease families in seven clans (as of 2009), where the clan AA with 6 families play a great importance.

Important aspartic proteases

  • Pepsin (A1)
  • Chymosin ( rennin, A1)
  • Renin ( A1)
  • Presenilin (A22 )
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